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Conserved domains on  [gi|164656228|ref|XP_001729242|]
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hypothetical protein MGL_3709 [Malassezia globosa CBS 7966]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAGA-Tad1 super family cl15080
Transcriptional regulator of RNA polII, SAGA, subunit; The yeast SAGA complex is a ...
 19-80 5.61e-13

Transcriptional regulator of RNA polII, SAGA, subunit; The yeast SAGA complex is a multifunctional coactivator that regulates transcription by RNA polymerase II. It is formed of five major modular subunits and shows a high degree of structural conservation to human TFTC and STAGA. The complex can also be conceived of as consisting of two histone-fold-containing core subunits, and this family is one of these. As a family it is likely to carry binding regions for interactions with a number of the other components of the complex.


The actual alignment was detected with superfamily member pfam12767:

Pssm-ID: 463692  Cd Length: 135  Bit Score: 65.96  E-value: 5.61e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164656228   19 VDPRAVKVRLFEKLG-SFADEYWQLLGALCTAAIDRAEFHNRVKAKLPSECVPLHNALVLSIL 80
Cdd:pfam12767   2 IDLEELKTQLKKKLGpERWEKYFEALSRFLSGKLSKAELDKLCDPILGRENLHLHNQLILSIL 64
HFD_SF super family cl45933
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 246-334 1.84e-11

histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally conserved interaction motif involved in heterodimerization of the core histones and their assembly into the nucleosome octamer. Histone fold heterodimers play crucial roles in gene regulation. The minimal HFD consists of three alpha helices connected by two short, unstructured loops. The HFD is found in core histones, TATA box-binding protein-associated factors (TAFs), and many other transcription factors. HFD plays a role in the nucleosomal core particle by conserving histone interactions; these contain more than one HFD. The structure of the nucleosome core particle has two modes that have the largest interaction surfaces, and these are the H3-H4 and H2A-H2B heterodimer interactions. Several TAFs interact via histone-fold (HF) motifs. Five HF-containing TAF pairs have been described in transcription factor II D (TFIID): TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10.


The actual alignment was detected with superfamily member cd22933:

Pssm-ID: 480273  Cd Length: 87  Bit Score: 59.92  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164656228 246 CIESQVLPDVHSLQDRMSLSAIEAGLSGGVHAHAAAVALSALHDYLQNILRRTflYTKKHARSTagaSRITMRDIMAVLD 325
Cdd:cd22933    2 CSESKELPDADSLRERMTGIALENGLLGGVAEECVELLLLALEQHLKNILSSC--IDKVRARRT---STLTLEDLLLALE 76


                 ....*....
gi 164656228 326 LAPHLIVEP 334
Cdd:cd22933   77 INPHLLGED 85
 
Name Accession Description Interval E-value
SAGA-Tad1 pfam12767
Transcriptional regulator of RNA polII, SAGA, subunit; The yeast SAGA complex is a ...
 19-80 5.61e-13

Transcriptional regulator of RNA polII, SAGA, subunit; The yeast SAGA complex is a multifunctional coactivator that regulates transcription by RNA polymerase II. It is formed of five major modular subunits and shows a high degree of structural conservation to human TFTC and STAGA. The complex can also be conceived of as consisting of two histone-fold-containing core subunits, and this family is one of these. As a family it is likely to carry binding regions for interactions with a number of the other components of the complex.


Pssm-ID: 463692  Cd Length: 135  Bit Score: 65.96  E-value: 5.61e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164656228   19 VDPRAVKVRLFEKLG-SFADEYWQLLGALCTAAIDRAEFHNRVKAKLPSECVPLHNALVLSIL 80
Cdd:pfam12767   2 IDLEELKTQLKKKLGpERWEKYFEALSRFLSGKLSKAELDKLCDPILGRENLHLHNQLILSIL 64
HFD_HFI1 cd22933
histone-fold domain found in transcriptional coactivator HFI1 and similar proteins; HFI1, also ...
 246-334 1.84e-11

histone-fold domain found in transcriptional coactivator HFI1 and similar proteins; HFI1, also called ADA1, is a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA (Spt-Ada-Gcn5-acetyltransferase) is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TATA binding protein (TBP) interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA (SAGA altered, SPT8 absent), an altered form of SAGA, may be involved in positive transcriptional regulation. Besides lacking SPT8, SALSA contains an SPT7 subunit that is truncated. SLIK (SAGA-like) is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. HFI1/ADA1 and SPT20/ADA5 may recruit TATA binding protein (TBP) and possibly other basal factors to bind to the TATA box.


Pssm-ID: 467057  Cd Length: 87  Bit Score: 59.92  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164656228 246 CIESQVLPDVHSLQDRMSLSAIEAGLSGGVHAHAAAVALSALHDYLQNILRRTflYTKKHARSTagaSRITMRDIMAVLD 325
Cdd:cd22933    2 CSESKELPDADSLRERMTGIALENGLLGGVAEECVELLLLALEQHLKNILSSC--IDKVRARRT---STLTLEDLLLALE 76


                 ....*....
gi 164656228 326 LAPHLIVEP 334
Cdd:cd22933   77 INPHLLGED 85
SAGA-Tad1 pfam12767
Transcriptional regulator of RNA polII, SAGA, subunit; The yeast SAGA complex is a ...
 238-299 5.55e-08

Transcriptional regulator of RNA polII, SAGA, subunit; The yeast SAGA complex is a multifunctional coactivator that regulates transcription by RNA polymerase II. It is formed of five major modular subunits and shows a high degree of structural conservation to human TFTC and STAGA. The complex can also be conceived of as consisting of two histone-fold-containing core subunits, and this family is one of these. As a family it is likely to carry binding regions for interactions with a number of the other components of the complex.


Pssm-ID: 463692  Cd Length: 135  Bit Score: 51.71  E-value: 5.55e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164656228  238 KRSVATPNCIESQVLPDVHSLQDRMSLSAIEAGLSGGVHAHAAAVALSALHDYLQNILRRTF 299
Cdd:pfam12767  71 RSPYAAPLAYESGELPDTDSLRKRMEPIAYEHGLVGGVSADCANLLNNALDVYLKNLLESCI 132
 
Name Accession Description Interval E-value
SAGA-Tad1 pfam12767
Transcriptional regulator of RNA polII, SAGA, subunit; The yeast SAGA complex is a ...
 19-80 5.61e-13

Transcriptional regulator of RNA polII, SAGA, subunit; The yeast SAGA complex is a multifunctional coactivator that regulates transcription by RNA polymerase II. It is formed of five major modular subunits and shows a high degree of structural conservation to human TFTC and STAGA. The complex can also be conceived of as consisting of two histone-fold-containing core subunits, and this family is one of these. As a family it is likely to carry binding regions for interactions with a number of the other components of the complex.


Pssm-ID: 463692  Cd Length: 135  Bit Score: 65.96  E-value: 5.61e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164656228   19 VDPRAVKVRLFEKLG-SFADEYWQLLGALCTAAIDRAEFHNRVKAKLPSECVPLHNALVLSIL 80
Cdd:pfam12767   2 IDLEELKTQLKKKLGpERWEKYFEALSRFLSGKLSKAELDKLCDPILGRENLHLHNQLILSIL 64
HFD_HFI1 cd22933
histone-fold domain found in transcriptional coactivator HFI1 and similar proteins; HFI1, also ...
 246-334 1.84e-11

histone-fold domain found in transcriptional coactivator HFI1 and similar proteins; HFI1, also called ADA1, is a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA (Spt-Ada-Gcn5-acetyltransferase) is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TATA binding protein (TBP) interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA (SAGA altered, SPT8 absent), an altered form of SAGA, may be involved in positive transcriptional regulation. Besides lacking SPT8, SALSA contains an SPT7 subunit that is truncated. SLIK (SAGA-like) is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. HFI1/ADA1 and SPT20/ADA5 may recruit TATA binding protein (TBP) and possibly other basal factors to bind to the TATA box.


Pssm-ID: 467057  Cd Length: 87  Bit Score: 59.92  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164656228 246 CIESQVLPDVHSLQDRMSLSAIEAGLSGGVHAHAAAVALSALHDYLQNILRRTflYTKKHARSTagaSRITMRDIMAVLD 325
Cdd:cd22933    2 CSESKELPDADSLRERMTGIALENGLLGGVAEECVELLLLALEQHLKNILSSC--IDKVRARRT---STLTLEDLLLALE 76


                 ....*....
gi 164656228 326 LAPHLIVEP 334
Cdd:cd22933   77 INPHLLGED 85
SAGA-Tad1 pfam12767
Transcriptional regulator of RNA polII, SAGA, subunit; The yeast SAGA complex is a ...
 238-299 5.55e-08

Transcriptional regulator of RNA polII, SAGA, subunit; The yeast SAGA complex is a multifunctional coactivator that regulates transcription by RNA polymerase II. It is formed of five major modular subunits and shows a high degree of structural conservation to human TFTC and STAGA. The complex can also be conceived of as consisting of two histone-fold-containing core subunits, and this family is one of these. As a family it is likely to carry binding regions for interactions with a number of the other components of the complex.


Pssm-ID: 463692  Cd Length: 135  Bit Score: 51.71  E-value: 5.55e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164656228  238 KRSVATPNCIESQVLPDVHSLQDRMSLSAIEAGLSGGVHAHAAAVALSALHDYLQNILRRTF 299
Cdd:pfam12767  71 RSPYAAPLAYESGELPDTDSLRKRMEPIAYEHGLVGGVSADCANLLNNALDVYLKNLLESCI 132
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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